Monteleone Stefania, Morao Inaki, Fedorov Dmitri G, Kellici Tahsin F
Drug Discovery, Evotec (U.K.) Ltd., 95 Park Drive, Milton Park, Abingdon, OX14 4RY, United Kingdom.
Protein Homeostasis, Evotec (U.K.) Ltd., 114 Innovation Drive, Milton Park, Abingdon, OX14 4RZ, United Kingdom.
ACS Med Chem Lett. 2025 Feb 6;16(3):420-427. doi: 10.1021/acsmedchemlett.4c00534. eCollection 2025 Mar 13.
Targeted protein degradation has become the most pursued alternative modality to small-molecule inhibition over the past decade. The traditional strategy of blocking protein activity by tightly binding to a functional substrate pocket has progressed toward proteolysis-targeting chimeras (PROTACs), bivalent molecules that induce the knockdown of targeted proteins. Herein, a combined protocol is described for modeling ternary complexes via well-established approaches. We performed local protein-protein docking using Rosetta protocol and sampled the conformational landscape of a specific PROTAC molecule that was compatible with the generated protein-protein docking poses, followed by double and independent single-linkage/nearest-neighbor clustering for representative selection. Subsequently, we combined the fragment molecular orbital and density functional tight-binding methods to facilitate fast quantum mechanics-based energy calculations of the clustered ternary complexes. Finally, the computed energy values were utilized to score and select the best ternary poses, achieving good agreement with available crystallographic data.
在过去十年中,靶向蛋白质降解已成为小分子抑制之外最受关注的替代方式。通过紧密结合功能性底物口袋来阻断蛋白质活性的传统策略已发展为靶向蛋白水解嵌合体(PROTACs),即诱导靶向蛋白质敲低的二价分子。本文描述了一种通过成熟方法对三元复合物进行建模的组合方案。我们使用Rosetta协议进行局部蛋白质-蛋白质对接,并对与生成的蛋白质-蛋白质对接姿势兼容的特定PROTAC分子的构象景观进行采样,然后通过双重和独立的单链/最近邻聚类进行代表性选择。随后,我们结合片段分子轨道和密度泛函紧束缚方法,以促进基于量子力学的聚类三元复合物的快速能量计算。最后,利用计算出的能量值对最佳三元姿势进行评分和选择,与现有的晶体学数据取得了良好的一致性。